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Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers
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| Zeitschriftentitel: | American Journal of Physiology-Cell Physiology |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | American Journal of Physiology-Cell Physiology, 291, 2006, 2, S. C245-C253 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
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| Schlagwörter: |
| author_facet |
Nori, Alessandra Valle, Giorgia Bortoloso, Elena Turcato, Federica Volpe, Pompeo Nori, Alessandra Valle, Giorgia Bortoloso, Elena Turcato, Federica Volpe, Pompeo |
|---|---|
| author |
Nori, Alessandra Valle, Giorgia Bortoloso, Elena Turcato, Federica Volpe, Pompeo |
| spellingShingle |
Nori, Alessandra Valle, Giorgia Bortoloso, Elena Turcato, Federica Volpe, Pompeo American Journal of Physiology-Cell Physiology Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers Cell Biology Physiology |
| author_sort |
nori, alessandra |
| spelling |
Nori, Alessandra Valle, Giorgia Bortoloso, Elena Turcato, Federica Volpe, Pompeo 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.00370.2005 <jats:p>Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lumen of terminal cisternae (TC) of the sarcoplasmic reticulum (SR). The physiological role of CS in controlling calcium release from the SR depends on both its intrinsic properties and its localization. The mechanisms of CS targeting were investigated in skeletal muscle fibers and C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, a model of SR differentiation, with four deletion mutants of epitope (hemagglutinin, HA)-tagged CS: CS-HAΔ24<jats:sub>NH2</jats:sub>, CS-HAΔ2D, CS-HAΔ3D, and CS-HAΔHT, a double mutant of the NH<jats:sub>2</jats:sub>terminus and domain III. As judged by immunofluorescence of transfected skeletal muscle fibers, only the double CS-HA mutant showed a homogeneous distribution at the sarcomeric I band, i.e., it did not segregate to TC. As shown by subfractionation of microsomes derived from transfected skeletal muscles, CS-HAΔHT was largely associated to longitudinal SR whereas CS-HA was concentrated in TC. In C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, as judged by immunofluorescence, not only CS-HAΔHT but also CS-HAΔ3D and CS-HAΔ2D were not sorted to developing SR. Condensation competence, a property referable to CS oligomerization, was monitored for the several CS-HA mutants in C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myoblasts, and only CS-HAΔ3D was found able to condense. Together, the results indicate that 1) there are at least two targeting sequences at the NH<jats:sub>2</jats:sub>terminus and domain III of CS, 2) SR-specific target and structural information is contained in these sequences, 3) heterologous interactions with junctional SR proteins are relevant for segregation, 4) homologous CS-CS interactions are involved in the overall targeting process, and 5) different targeting mechanisms prevail depending on the stage of SR differentiation.</jats:p> Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers American Journal of Physiology-Cell Physiology |
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| title |
Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_unstemmed |
Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_full |
Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_fullStr |
Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_full_unstemmed |
Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_short |
Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_sort |
calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| topic |
Cell Biology Physiology |
| url |
http://dx.doi.org/10.1152/ajpcell.00370.2005 |
| publishDate |
2006 |
| physical |
C245-C253 |
| description |
<jats:p>Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lumen of terminal cisternae (TC) of the sarcoplasmic reticulum (SR). The physiological role of CS in controlling calcium release from the SR depends on both its intrinsic properties and its localization. The mechanisms of CS targeting were investigated in skeletal muscle fibers and C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, a model of SR differentiation, with four deletion mutants of epitope (hemagglutinin, HA)-tagged CS: CS-HAΔ24<jats:sub>NH2</jats:sub>, CS-HAΔ2D, CS-HAΔ3D, and CS-HAΔHT, a double mutant of the NH<jats:sub>2</jats:sub>terminus and domain III. As judged by immunofluorescence of transfected skeletal muscle fibers, only the double CS-HA mutant showed a homogeneous distribution at the sarcomeric I band, i.e., it did not segregate to TC. As shown by subfractionation of microsomes derived from transfected skeletal muscles, CS-HAΔHT was largely associated to longitudinal SR whereas CS-HA was concentrated in TC. In C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, as judged by immunofluorescence, not only CS-HAΔHT but also CS-HAΔ3D and CS-HAΔ2D were not sorted to developing SR. Condensation competence, a property referable to CS oligomerization, was monitored for the several CS-HA mutants in C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myoblasts, and only CS-HAΔ3D was found able to condense. Together, the results indicate that 1) there are at least two targeting sequences at the NH<jats:sub>2</jats:sub>terminus and domain III of CS, 2) SR-specific target and structural information is contained in these sequences, 3) heterologous interactions with junctional SR proteins are relevant for segregation, 4) homologous CS-CS interactions are involved in the overall targeting process, and 5) different targeting mechanisms prevail depending on the stage of SR differentiation.</jats:p> |
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| author | Nori, Alessandra, Valle, Giorgia, Bortoloso, Elena, Turcato, Federica, Volpe, Pompeo |
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| description | <jats:p>Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lumen of terminal cisternae (TC) of the sarcoplasmic reticulum (SR). The physiological role of CS in controlling calcium release from the SR depends on both its intrinsic properties and its localization. The mechanisms of CS targeting were investigated in skeletal muscle fibers and C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, a model of SR differentiation, with four deletion mutants of epitope (hemagglutinin, HA)-tagged CS: CS-HAΔ24<jats:sub>NH2</jats:sub>, CS-HAΔ2D, CS-HAΔ3D, and CS-HAΔHT, a double mutant of the NH<jats:sub>2</jats:sub>terminus and domain III. As judged by immunofluorescence of transfected skeletal muscle fibers, only the double CS-HA mutant showed a homogeneous distribution at the sarcomeric I band, i.e., it did not segregate to TC. As shown by subfractionation of microsomes derived from transfected skeletal muscles, CS-HAΔHT was largely associated to longitudinal SR whereas CS-HA was concentrated in TC. In C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, as judged by immunofluorescence, not only CS-HAΔHT but also CS-HAΔ3D and CS-HAΔ2D were not sorted to developing SR. Condensation competence, a property referable to CS oligomerization, was monitored for the several CS-HA mutants in C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myoblasts, and only CS-HAΔ3D was found able to condense. Together, the results indicate that 1) there are at least two targeting sequences at the NH<jats:sub>2</jats:sub>terminus and domain III of CS, 2) SR-specific target and structural information is contained in these sequences, 3) heterologous interactions with junctional SR proteins are relevant for segregation, 4) homologous CS-CS interactions are involved in the overall targeting process, and 5) different targeting mechanisms prevail depending on the stage of SR differentiation.</jats:p> |
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| imprint | American Physiological Society, 2006 |
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| institution | DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1 |
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| spelling | Nori, Alessandra Valle, Giorgia Bortoloso, Elena Turcato, Federica Volpe, Pompeo 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.00370.2005 <jats:p>Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lumen of terminal cisternae (TC) of the sarcoplasmic reticulum (SR). The physiological role of CS in controlling calcium release from the SR depends on both its intrinsic properties and its localization. The mechanisms of CS targeting were investigated in skeletal muscle fibers and C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, a model of SR differentiation, with four deletion mutants of epitope (hemagglutinin, HA)-tagged CS: CS-HAΔ24<jats:sub>NH2</jats:sub>, CS-HAΔ2D, CS-HAΔ3D, and CS-HAΔHT, a double mutant of the NH<jats:sub>2</jats:sub>terminus and domain III. As judged by immunofluorescence of transfected skeletal muscle fibers, only the double CS-HA mutant showed a homogeneous distribution at the sarcomeric I band, i.e., it did not segregate to TC. As shown by subfractionation of microsomes derived from transfected skeletal muscles, CS-HAΔHT was largely associated to longitudinal SR whereas CS-HA was concentrated in TC. In C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myotubes, as judged by immunofluorescence, not only CS-HAΔHT but also CS-HAΔ3D and CS-HAΔ2D were not sorted to developing SR. Condensation competence, a property referable to CS oligomerization, was monitored for the several CS-HA mutants in C<jats:sub>2</jats:sub>C<jats:sub>12</jats:sub>myoblasts, and only CS-HAΔ3D was found able to condense. Together, the results indicate that 1) there are at least two targeting sequences at the NH<jats:sub>2</jats:sub>terminus and domain III of CS, 2) SR-specific target and structural information is contained in these sequences, 3) heterologous interactions with junctional SR proteins are relevant for segregation, 4) homologous CS-CS interactions are involved in the overall targeting process, and 5) different targeting mechanisms prevail depending on the stage of SR differentiation.</jats:p> Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers American Journal of Physiology-Cell Physiology |
| spellingShingle | Nori, Alessandra, Valle, Giorgia, Bortoloso, Elena, Turcato, Federica, Volpe, Pompeo, American Journal of Physiology-Cell Physiology, Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers, Cell Biology, Physiology |
| title | Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_full | Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_fullStr | Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_full_unstemmed | Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_short | Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_sort | calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| title_unstemmed | Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers |
| topic | Cell Biology, Physiology |
| url | http://dx.doi.org/10.1152/ajpcell.00370.2005 |